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Phosphorylation of Fanconi anemia protein, FANCA, is regulated by Akt kinase.

Phosphorylation of the Fanconi anemia complementation group A (FANCA) protein is thought to be important for the function of the FA pathway. However, the kinase for FANCA (so-called FANCA-PK) remains to be identified. FANCA has a consensus sequence for Akt kinase near serine 1149 (Ser1149), suggesting that Akt can phosphorylate FANCA. We performed in vitro kinase assays using as substrate either a GST-fusion wild-type (WT) FANCA fragment or a GST-fusion FANCA fragment containing a mutation from serine to alanine at 1149 (FANCA-S1149A). These experiments confirmed that FANCA is phosphorylated at Ser 1149, in vitro. However, (32)P-orthophosphate labeling experiments revealed that FANCA-S1149A was more efficiently phosphorylated than WT-FANCA. Furthermore, phosphorylation of wild-type FANCA was blocked by coexpression of a constitutively active (CA)-Akt and enhanced by a dominant-negative (DN) Akt. Our results suggest that Akt is a negative regulator of FANCA phosphorylation.

Pubmed ID: 11855836

Authors

  • Otsuki T
  • Nagashima T
  • Komatsu N
  • Kirito K
  • Furukawa Y
  • Kobayashi Si S
  • Liu JM
  • Ozawa K

Journal

Biochemical and biophysical research communications

Publication Data

March 1, 2002

Associated Grants

None

Mesh Terms

  • Amino Acid Sequence
  • Cell Line
  • Consensus Sequence
  • DNA-Binding Proteins
  • Fanconi Anemia Complementation Group A Protein
  • Genetic Complementation Test
  • Humans
  • Phosphorylation
  • Precipitin Tests
  • Protein-Serine-Threonine Kinases
  • Proteins
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-akt